Fibrinogen and fibrin - Proteins with complex roles in hemostasis and thrombosis

Thrombosis Research

Volumn 83, Issue 1, 1996, Pages 1-75

  Blombäck, Birger ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

biosynthesis; evolution; fibrin; Fibrinogen; fibrinolysis; platelets; thrombosis

Indexed keywords

FIBRIN; FIBRINOGEN; THROMBIN;

BLOOD CLOTTING; DISULFIDE BOND; ELECTRON MICROSCOPY; FIBRIN FORMATION; FIBRIN POLYMERIZATION; FIBRINOGEN SYNTHESIS; HEMOSTASIS; HUMAN; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DETERMINATION; PROTEIN POLYMERIZATION; REVIEW; THROMBOCYTE ADHESION; THROMBOGENESIS; THROMBOSIS;

EID: 0030199185     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/0049-3848(96)00111-9     Document Type: Article

References (443)

1. BAILEY K., BETTELHEIM F.R., LORAND L., MIDDLEBROOK W.R. Action of thrombin in the clotting of fibrinogen. Nature. 167:1951;233-234.
2. BAILEY K., BETTELHEIM F.R. The clotting of fibrinogen. I. The liberation of peptide material Biochim Biophys Acta. 18:1955;495-503.
3. SCHERAGA H.A., LASKOWSKI M. JR. The fibrinogen-fibrin conversion. Adv Protein Chem. 12:1957;1-131.
4. BLOMBÄCK, B. Fibrinogen to fibrin transformation. In: Blood Clotting Enzymology. W.H. Seegers (ed.), pp. 143-215, Academic Press Inc., New York 1967.
5. LAKI, K. Introduction and summary. In: Fibrinogen. K. Laki (ed.), pp. 1-24, Marcel Dekker Inc., New York 1968.
6. DOOLITTLE R.F. Fibrinogen and fibrin. Annu Rev Biochem. 53:1984;195-229.
7. FURLAN, M. Structure and function of normal fibrinogen. In: Variants of Human Fibrinogen. E.A. Beck and M. Furlan (eds.), pp. 38-63, Hans Huber Publishers, Toronto 1984.
8. CRABTREE, G.R. The molecular biology of fibrinogen. In: The Molecular Basis of Blood Diseases. G. Stamatoyannopoulos, A.W. Nienhuis, P. Leder, P.W. Majerus (eds.), pp. 631-661, W.B. Saunders Co., Philadelphia 1987.
9. CASPARY E.A., KEKWICK R.A. Some physicochemical properties of human fibrinogen. Biochem J. 67:1957;41-48.
10. FU Y., WEISSBACH L., PLANT P.W., ODDOUX C., CAO Y., LIANG T.J., ROY S.N., REDMAN C.M., GRIENINGER G. Carboxy-terminal-extended variant of the human fibrinogen α subunit: A novel exon conferring marked homology to β and γ subunits. Biochemistry. 31:1992;11968-11972.
11. 420: A normal human variant with two extended a chains. Proc Natl Acad Sci USA. 91:1994;2625-2628.
12. MARGUERIE G., STUHRMANN H.B. A neutron small-angle scattering study of bovine fibrinogen. J Mol Biol. 102:1976;143-156.
13. HALL C.E., SLAYTER H.S. The fibrinogen molecule: Its size, shape and mode of polymerization. J Biophys Biochem Cytol. 5:1959;11-17.
14. STRYER L., COHEN C., LANGRIDGE R. Axial period of fibrinogen and fibrin. Nature. 197:1963;793-794.
15. TOONEY N.M., COHEN C. Microcrystals of a modified fibrinogen. Nature. 237:1972;23-25.
16. COHEN C., WEISEL J.W., PHILLIPS G.N. JR., STAUFFACHER C.V., FILLERS J.P., DAUB E. The structure of fibrinogen and fibrin. I. Electron microscopy and X-ray crystallography of fibrinogen Ann NY Acad Sci. 408:1983;194-213.
17. WEISEL J.W., STAUFFACHER C.V., BULLITT E., COHEN C. A model for fibrinogen: Domains and sequence. Science. 230:1985;1388-1391.
18. BACHMANN L., SCHMITT-FURMIAN W.W., HAMMEL R., LEDERER K. Size and shape of fibrinogen. I. Electron microscopy of the hydrated molecule Macromol Chemie. 176:1975;2603-2618.
19. MOSESSON M.W. Fibrinogen heterogeneity. Ann NY Acad Sci. 408:1983;97-113.
20. HOLM B., NILSEN D.W.T., KIERULF P., GODAL H.C. Purification and characterization of 3 fibrinogens with different molecular weights obtained from normal human plasma. Thromb Res. 37:1985;165-176.
21. HOLM B., BROSSTAD F., KIERULF P., GODAL H.C. Polymerization properties of two normally circulating fibrinogens, HMW and LMW. Evidence that the COOH-terminal end of the α-chain is of importance for fibrin polymerization. Thromb Res. 39:1985;595-606.
22. GAFFNEY P.J. Structure of fibrinogen and degradation products of fibrinogen and fibrin. Br Med Bull. 33:1977;245-252.
23. BACH-GANSMO E.T., HALVORSEN S., GODAL H.C., SKJØNSBERG O.H. Impaired coagulation of fibrinogen due to digestion of the C-terminal end of the Aα-chain by human neutrophil elastases. Thromb Res. 73:1994;61-68.
24. NOSSEL H.L. Relative proteolysis of the fibrinogen Bβ chain by thrombin and plasmin as a determinant of thrombosis. Nature. 291:1981;165-167.
25. FINLAYSON J.S., MOSESSON M.W. Heterogeneity of human fibrinogen. Biochemistry. 2:1963;42-46.
26. MOSHER D.F., BLOUT E.R. Heterogeneity of bovine fibrinogen and fibrin. J Biol Chem. 248:1973;6896-6903.
27. MOSESSON M.W., FINLAYSON J.S., UMFLEET R.A. Human fibrinogen heterogeneities. III. Identification of γ chain variants J Biol Chem. 247:1972;5223-5227.
28. GAFFNEY P.J. Localisation of carbohydrate in the subunits of human fibrinogen and its plasmin induced fragments. Biochim Biophys Acta. 263:1972;453-458.
29. GATI W.P., STRAUB P.W. Separation of both the Bβ- and the γ-polypeptide chains of human fibrinogen into two main types which differ in sialic acid content. J Biol Chem. 253:1978;1315-1321.
30. EBERT, R.F. Index of Variant Human Fibrinogens. CRC Press, Inc., Boca Raton, Ann Arbor, London, Tokyo 1994.
31. BLOMBÄCK B., YAMASHINA I. On the N-terminal amino acids in fibrinogen and fibrin. Arkiv Kemi. 12:1958;299-319.
32. BLOMBÄCK B., BLOMBÄCK M., HENSCHEN A., HESSEL B., IWANAGA S., WOODS K.R. N-terminal disulphide knot of human fibrinogen. Nature. 218:1968;130-134.
33. BLOMBÄCK B. The N-terminal disulphide knot of human fibrinogen. The Fourth Michael Cross Memorial Lecture, London. Br J Haematol. 17:1969;145-157.
34. 2-terminal part of human fibrinogen. Thromb Res. 8:1976;639-658.
35. HENSCHEN A. Paper electrophoretic patterns and mobilities of unmodified, sulfitolyzed and reduced and alkylated fibrinogen and fibrin in buffered 6 M urea. Arkiv Kemi. 22:1964;397-415.
36. MIYATA T., TERUKINA S., MATSUDA M., KASAMATSU A., TAKEDA Y., MURAKAMI T., IWANAGA S. Fibrinogens Kawaguchi and Osaka: An amino acid substitution of Aα arginine 16 to cysteine which forms an extra interchain disulfide bridge between the two Aα chains. J Biochem. 102:1987;93-101.
37. HOEPRICH H.D., DOOLITTLE R.F. Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation. Biochemistry. 22:1983;2049-2055.
38. HENSCHEN, A., LOTTSPECH, F., KEHL, M., SOUTHAN, D. and LUCAS, J. Structure-function-evolution relationship in fibrinogen. In: Fibrinogen-Recent Biochemical and Medical Aspects. A. Henschen, H. Graeff and F. Lottspech (eds.), pp. 67-82, Walter de Gruyter & Co., Berlin-New York 1982.
39. HENSCHEN A., LOTTSPEICH F., KEHL M., SOUTHAN C. Covalent structure of fibrinogen. Ann NY Acad Sci. 408:1983;28-43.
40. DOOLITTLE R.F. The structure and evolution of vertebrate fibrinogen. Ann NY Acad Sci. 408:1983;13-27.
41. WATT K.W.K., COTTRELL B.A., STRONG D.D., DOOLITTLE R.F. Amino acid sequence studies on the α chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry. 18:1979;5410-5416.
42. KANT J.A., LORD S.T., CRABTREE J.R. Partial mRNA sequences for human Aα, Bβ, and γ fibrinogen chains: Evolutionary and functional implications. Proc Natl Acad Sci USA. 80:1983;3953-3957.
43. WOLFENSTEIN-TODEL C., MOSESSON M.W. Carboxy-terminal amino acid sequence of a human fibrinogen γ-chain variant (γ′). Biochemistry. 20:1981;6146-6149.
44. CRABTREE G.R., KANT J.A. Organization of the rat gamma-fibrinogen gene: Alternative mRNA splice patterns produce the gamma A and gamma B (gamma ′) chains of fibrinogen. Cell. 31:1982;159-166.
45. FORNACE A.J. JR., CUMMINGS D.E., COMEAU C.M., KANT J.A., CRABTREE G.R. Structure of the human γ-fibrinogen gene. J Biol Chem. 259:1983;12826-12830.
46. FRANCIS C.W., MÜLLER E., HENSCHEN A., SIMPSON P.J., MARDER V.J. V.J. Carboxyl-terminal amino acid sequences of two variant forms of the γ chain of human plasma fibrinogen. Proc Natl Acad Sci USA. 85:1988;3358-3362.
47. SEYDEWITZ H.H., WITT I. Increased phosphorylation of human fibrinopeptide A under acute phase conditions. Thromb Res. 40:1985;29-39.
48. KRAJEWSKI T., BLOMBÄCK B. The location of tyrosine-O-S in fibrinopeptides. Acta Chem Scand. 22:1968;1339-1346.
49. JEVONS F.R. Tyrosine O-sulphate in fibrinogen and fibrin. Biochem J. 89:1963;621-624.
50. FARRELL D.H., MULVIHILL E.R., HUANG S., CHUNG D.W., DAVIE E.W. Recombinant human fibrinogen and sulfation of the γ′ chain. Biochemistry. 30:1991;9414-9420.
51. 1H-NMR to characterize glycosidase-treated glycopeptides. J Biol Chem. 257:1982;9704-9710.
52. MESTER L. Structure and the role of carbohydrate fractions of glycoproteins implicated in blood coagulation. Bull Soc Chim Biol. 51:1969;635-648.
53. BLOMBÄCK B., GRÖNDAHL N.J., HESSEL B., IWANAGA S., WALLÉN P. Primary structure of human fibrinogen and fibrin. J Biol Chem. 248:1973;5806-5820.
54. WATT K.W.K., TAKAGI T., DOOLITTLE R.F. Amino acid sequence of the β chain of human fibrinogen. Biochemistry. 18:1979;68-76.
55. EVERSE S.J., PELLETIER H., DOOLITTLE R.F. Crystallization of fragment D from human fibrinogen. Protein Sci. 4:1995;1013-1016.
56. GÅRDLUND B., HESSEL B., MARGUERIE G., MURANO G., BLOMBÄCK B. Chemical characterization of disulfide containing cyanogen bromide fragments. Eur J Biochem. 77:1977;595-610.
57. BLOMBÄCK B., BLOMBÄCK M., OLSSON P., SVENDSEN L., ÅBERG G. Synthetic peptides with anticoagulant and vasodilating activity. Scand J Clin Lab Inv. 24(Suppl. 107):1969;59-64.
58. BLOMBÄCK B., BLOMBÄCK M., FINKBEINER W., HOLMGREN A., KOWALSKA-LOTH B., OLOVSON G. Enzymatic reduction of disulfide bonds in fibrinogen by the thioredoxin system. I. Identification of reduced bonds and studies on reoxidation process Thromb Res. 4:1974;55-75.
59. PROCYK R., BLOMBÄCK B. Disulfide bond reduction in fibrinogen: Calcium protection and effect on clottability. Biochemistry. 29:1990;1501-1507.
60. PROCYK R., MEDVED L., ENGELKE K.J., KUDRYK B., BLOMBÄCK B. Nonclottable fibrin obtained from partially reduced fibrinogen: Characterization and tissue plasminogen activator stimulation. Biochemistry. 31:1992;2273-2278.
61. ZHANG J.-Z., REDMAN C.M. Role of interchain disulfide bonds on the assembly and secretion of human fibrinogen. J Biol Chem. 269:1994;652-658.
62. HUANG S., CAO Z., DAVIE E.W. The role of amino-terminal disulfide bonds in the structure and assembly of human fibrinogen. Biochem Biophys Res Commun. 190:1993;488-495.
63. BOUMA H. III, TAKAGI T., DOOLITTLE R.F. The arrangement of disulfide bonds in fragment D from human fibrinogen. Thromb Res. 13:1978;557-562.
64. DOOLITTLE R.F., GOLDBAUM D.M., DOOLITTLE L.R. Designation of sequences involved in the "coiled coil" interdomanial connections in fibrinogen: Construction of an atomic scale model. J Mol Biol. 120:1978;311-325.
65. KOWALSKA-LOTH B., GÅRDLUND B., EGBERG N., BLOMBÄCK B. Plasmic degradation products of human fibrinogen. II. Chemical and immunological relation between fragment E and N-DSK Thromb Res. 2:1973;423-450.
66. COLLEN D., KUDRYK B., HESSEL B., BLOMBÄCK B. Primary structure of human fibrinogen and fibrin. III. Isolation and partial characterization of chains of fragment D J Biol Chem. 250:1975;5808-5817.
67. GÅDLUND B. Human fibrinogen-amino acid sequence of fragment E and of adjacent structures in the Aα- and Bβ-chains. Thromb Res. 10:1977;689-702.
68. DOOLITTLE R.F., WATT K.W.K., COTTRELL B.A., STRONG D.D., RILEY M. The amino acid sequence of the α-chain of human fibrinogen. Nature. 280:1979;464-468.
69. BLOMBÄCK B., HESSEL B., HOGG D., THERKILDSEN L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature. 257:1978;501-505.
70. BLOMBÄCK B., VESTERMARK A. Isolation of fibrinopeptides by chromatography. Arkiv Kemi. 12:1958;173-182.
71. BLOMBÄCK B., OKADA M., FORSLIND B., LARSSON U. Fibrin gels as biological filters and interfaces. Biorheology. 21:1984;93-104.
72. SHAINOFF J.R., SMEJKAL G.B., DiBELLO P.M., BULLOCH R.E., LEVY P.J., JANG Y., LILL H. A nonaggregating fibrin-precursor identified in abnormal plasmas and thrombin reactions. Thromb Haemost. 73(1242 Abs.):1995;1225.
73. MEH D.A., SIEBENLIST K.R., BERGTROM G., MOSESSON M.M. Sequence of release of fibrinopeptide A from fibrinogen molecules by thrombin or Atroxin. J Lab Clin Med. 125:1995;384-391.
74. BLOMBÄCK B., OKADA M. Fibrin gel structure and clotting time. Thromb Res. 25:1982;51-70.
75. OKADA M., BLOMBÄCK B. Calcium and fibrin gel structure. Thromb Res. 29:1983;269-280.
76. BARK N., BLOMBÄCK B., FATAH K. On the occurrence of thrombin-like enzymes in mosquitoes. Thromb Res. 81:1996;623-634.
77. WEISEL J.W. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 50:1986;1079-1093.
78. WEISEL J.W., VEKLICH Y., GORKUN O. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J Mol Biol. 232:1993;285-297.
79. BLOMBÄCK, B. Fibrinogen and fibrin formation. In: Handbuch der Experimentellen Pharmakologie. Vol. 46. Fibrinolytics and antifibrinolytics. F. Markward (ed.), pp. 49-79. Springer Verlag, Berlin-Heidelberg 1978.
80. HOGG D.H., BLOMBÄCK B. The mechanism of the fibrinogen-thrombin reaction. Thromb Res. 12:1978;953-964.
81. SIEBENLIST K.R., DiORIO J.P., BUDZYNSKI A.Z., MOSESSON M.W. The polymerization and thrombin-binding properties of Des-(Bβ21-42)-fibrin. J Biol Chem. 365:1990;18650-18655.
82. BLOMBÄCK B., BLOMBÄCK M., GRÖNDAHL N.J., HOLMBERG E. Structure of fibrinopeptides - its relation to enzyme specificity and phylogeny and classification of species. Arkiv Kemi. 25:1966;411-428.
83. SEEGERS W.H., NIEFT M., LOOMIS E.C. Note on the adsorption of thrombin on fibrin. Science. 101:1945;520-521.
84. CLAESON G. Synthetic peptides and peptidomimetics as substrates and inhibitors of thrombin and other proteases in the blood coagulation system. Blood Coag Fibrinol. 5:1994;411-436.
85. SCHERAGA, H.A. Chemistry and Biology of Thrombin. R.L Lundblad, J.W. Fenton, II and K.G. Mann (eds.), p. 145, Ann Arbor Science Publishers, Ann Arbor, MI 1977.
86. MEINWALD Y.C., MARTINELLI R.A., VAN NISPEN J.W., SCHERAGA H.A. Mechanism of action of thrombin on fibrinogen. Size of the Aα fibrinogen-like peptide that contacts the active site of thrombin. Biochemistry. 19:1980;3820-3825.
87. 10. Biochemistry. 22:1983;4170-4174.
88. NI F., KONISHI Y., FRAZIER R.B., SCHERAGA H.A., LORD S.T. High-resolution NMR studies of fibrinogen-like peptides in solution: Interaction of thrombin with residues 1-23 of the Aα chain of human fibrinogen. Biochemistry. 28:1989;3082-3094.
89. NI F., MEINWALD Y.C., VÁSQUEZ M., SCHERAGA H.A. High-resolution NMR studies of fibrinogen-like peptides in solution: Structure of a thrombin-bound peptide corresponding to residues 7-16 of the Aα chain of human fibrinogen. Biochemistry. 28:1989;3094-3105.
90. NI F., KONISHI Y., BULLOCK L.D., RIVETNA M.N., SCHERAGA H.A. High-resolution NMR studies of fibrinogen-like peptides in solution: Structural basis for the bleeding disorder caused by a single mutation of Gly(12) to Val(12) in the Aα chain of human fibrinogen Rouen. Biochemistry. 28:1989;3106-3119.
91. LORD S.T., BYRD P.A., HEDE K.L., WEI D., COLBY T.J. Analysis of fibrinogen Aα-fusion proteins. Mutants which inhibit thrombin equivalently are not equally good substrates. J Biol Chem. 265:1990;838-843.
92. STUBBS M.T., OSCHKINAT H., MAYR I., HUBER R., ANGLIKER H., STONE S.R., BODE W. The interaction of thrombin with fibrinogen. - A structural basis for its specificity. Eur J Biochem. 206:1992;187-195.
93. STUBBS M.T., BODE W. A player of many parts: The spotlight falls on thrombin's structure. Thromb Res. 69:1993;1-58.
94. MARTIN P.D., ROBERTSON W., TURK D., HUBER R., BODE W., EDWARDS B.F.P. The structure of residues 7-16 of the Aα-chain of human fibrinogen bound to bovine thrombin at 2.3Å resolution. J Biol Chem. 267:1992;7911-7920.
95. LIU C.Y., NOSSEL H.L., KAPLAN K.L. The binding of thrombin by fibrin. J Biol Chem. 254:1979;10421-10425.
96. FENTON J.W. II, OLSON T.A., ZABINSKI M.P., WILNER G.D. Anion-binding exosite of human α-thrombin and fibrin(ogen) recognition. Biochemistry. 27:1988;7106-7112.
97. BERLINER L.J., SUGAWARA Y., FENTION J.W. II Human α-thrombin binding to nonpolymerized fibrin-Sepharose: Evidence for an anionic binding region. Biochemistry. 24:1985;7005-7009.
98. KACZMARECK E., McDONAGH J. Thrombin binding to the Aα, Bβ and γ-chains of fibrinogen and to their remnants contained in fragment E. J Biol Chem. 263:1988;13896-13900.
99. VALI Z., SCHERAGA H.A. Localization of the binding site on fibrin for the secondary binding site of thrombin. Biochemistry. 27:1988;1956-1963.
100. BINNIE C.G., LORD S.T. A synthetic analogue of fibrinogen α27-50 is an inhibitor of thrombin. Thromb Haemost. 65:1991;165-168.
101. FERRY J.D. The mechanism of polymerization of fibrinogen. Proc Natl Acad Sci USA. 38:1952;566-569.
102. ERICKSON H.P., FOWLER W.E. Electron microscopy of fibrinogen, its plasmic fragments and small polymers. Ann NY Acad Sci. 408:1983;146-163.
103. LAURENT T.C., BLOMBÄCK B. On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chem Scand. 12:1958;1875-1877.
104. HEENE D.L., MATTHIAS F.R. Adsorption of fibrinogen derivatives on insolubilized fibrinogen and fibrin monomers. Thromb Res. 2:1973;137-154.
105. BLOMBÄCK M., BLOMBÄCK B., MAMMEN E.F., PRASAD A.S. Fibrinogen Detroit - a molecular defect in the N-terminal disulphide knot of human fibrinogen. Nature. 218:1968;134-137.
106. SÖDERQVIST T., BLOMBÄCK B. Fibrinogen structure and evolution. Naturwissenschaften. 58:1971;16-23.
107. BLOMBÄCK, B. and BLOMBÄCK, M. The molecular structure of fibrinogen. In: The biological role of the clot stabilizing enzymes: Transglutaminase and factor XIII. Conference, N.Y. November 1971. K. Laki (ed.). Ann NY Acad Sci 202, 77-97, 1972.
108. BLOMBÄCK, B. and BLOMBÄCK, M. The molecular structure of fibrinogen. In: The biological role of the clot stabilizing enzymes: Transglutaminase and factor XIII. Conference, N.Y. November 1971. K. Laki (ed.). Ann NY Acad Sci 202, 77-97, 1972.
109. KUDRYK B., REUTERBY J., BLOMBÄCK B. Adsorption of plasmic fragment D to thrombin modified fibrinogen-Sepharose. Thromb Res. 2:1973;423-450.
110. KUDRYK B.J., COLLEN D., WOODS K.R., BLOMBÄCK B. Evidence for localization of polymerization sites in fibrinogen. J Biol Chem. 249:1974;3322-3325.
111. YORK L.L., BLOMBÄCK B. Interaction of fragments of fibrinogen with insolubilized fibrin monomers (activated fibrinogen). Thromb Res. 8:1976;607-618.
112. 2-terminal polymerization domain. Thromb Res. 9:1976;25-36.
113. LAUDANO A.P., DOOLITTLE R.F. Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. Biochemistry. 19:1978;1013-1019.
114. LAUDANO A.P., DOOLITTLE R.F. Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization to fibrin monomers. Proc Natl Acad Sci USA. 75:1978;3085-3089.
115. LAUDANO A.P., COTTRELL B.A., DOOLITTLE R.F. Synthetic peptides modeled on fibrin polymerization sites. Ann NY Acad Sci. 408:1983;315-329.
116. DRAY-ATTALI L., LARRIEU M.J. Fragments D-correlation between structure and biological activity. Thromb Res. 10:1977;575-586.
117. BUDZYNSKI A.Z., OLEXA S.A., PANDYA B.V. Fibrinogen polymerization sites in fibrinogen and fibrin fragments. Ann NY Acad Sci. 408:1983;301-314.
118. OLEXA S.A., BUDZYNSKI A.Z. Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci USA. 77:1980;1374-1378.
119. OLEXA S.A., BUDZYNSKI A.Z. Localization of a fibrin polymerization site. J Biol Chem. 256:1981;3544-3549.
120. VARADI A., SCHERAGA H.A. Localization of segments essential for polymerization and for calcium binding in the γ-chain of human fibrinogen. Biochemistry. 25:1986;519-528.
121. SHIMIZU A., NAGEL G.M., DOOLITTLE R.F. Photoaffinity labeling of the primary polymerization site: Isolation and characterization of a labeled cyanogen bromide fragment corresponding to γ-chain residues 337-379. Proc Natl Acad Sci USA. 89:1992;2888-2892.
122. YAMAZUMI K., DOOLITTLE R.F. Photoaffinity labeling of the primary fibrin polymerization site: Location of the label to γ-chain Tyr-363. Proc Natl Acad Sci USA. 89:1992;2893-2896.
123. BUDZYNSKI A.Z., STAHL M., KOPEC M., LATAOLLO Z.S., WEGRZYNOWICZ Z., KOWALSKI E. High molecular weight products of the late stage of fibrinogen proteolysis by plasmin and their structural relation with the fibrinogen molecule. Biochim Biophys Acta. 147:1967;313-323.
124. MIHALYI E. Clotting of bovine fibrinogen. Calcium binding to fibrin during clotting and its dependence on release of fibrinopeptide B. Biochemistry. 27:1988;967-976.
125. MIHALYI E. Clotting of bovine fibrinogen. Kinetic analysis of the release of fibrinopeptides by thrombin and of the calcium uptake upon clotting at high fibrinogen concentrations. Biochemistry. 27:1988;976-982.
126. MIHALYI E., TERCERO J.C., DIAZ-MAURINO T. Changes in pH associated with clotting of fibrinogen. Kinetic studies of the pH shift and correlation pH change with the release of fibrinopeptides and the ensuing polymerization. Biochemistry. 30:1991;4753-4762.
127. BLOMBÄCK, B., HESSEL, B., FIELDS, R. and PROCYK, R. Fibrinogen Aarhus: An abnormal fibrinogen with Aα19Arg → Gly substitution. In: Fibrinogen 3. Biochemistry, biological functions, gene regulation and expression. M.W. Mosesson et al. (eds.), pp. 263-266, Elsevier Science Publ. B.V. Biomedical Division, Amsterdam 1988.
128. BLOMBÄCK B. Studies on the action of thrombic enzymes on bovine fibrinogen as measured by N-terminal analysis. Arkiv Kemi. 12:1958;321-335.
129. HASEGAWA N., SASAKI S. Location of the binding site 'b' for lateral polymerization of fibrin. Thromb Res. 57:1990;183-195.
130. SHAINOFF J.R., DARDIK B.N. Fibrinopeptide B and aggregation of fibrinogen. Science. 204:1979;200-202.
131. SHAINOFF J.R., DARDIK B.N. Fibrinopeptide B in fibrin assembly and metabolism. Physiologic significance in delayed release of the peptide. Ann NY Acad Sci. 408:1983;254-268.
132. DYR J.E., BLOMBÄCK B., HESSEL B., KORNALIK F. Conversion of fibrinogen to fibrin induced by preferential release of fibrinopeptide B. Biochim Biophys Acta. 990:1989;18-24.
133. WEISEL J.W., FRANCIS C.W., NAGASWAMI C., MARDER V.J. Determination of the topology of factor XIIIa-induced fibrin γ-chain cross-links by electron microscopy of ligated fragments. J Biol Chem. 268:1993;26618-26624.
134. BLOMBÄCK B., CARLSSON K., FATAH K., HESSEL B., PROCYK R. Fibrin in human plasma: Gel architectures governed by rate and nature of fibrinogen activation. Thromb Res. 75:1994;521-538.
135. WEISEL J.W., NAGASWAMI C., MAKOWSKI L. Twisting of fibrin fibers limits their radial growth. Proc Natl Acad Sci USA. 84:1987;8991-8995.
136. MEDVED L.V. Relationship between exons and domains in the fibrinogen molecule. Blood Coagul Fibrinol. 1:1990;439-442.
137. VEKLICH Y.I., GORKUN O.V., MEDVED L.V., NIEUWENHUIZEN W., WEISEL J.W. Carboxy-terminal portions of the α-chains of fibrinogen and fibrin. Localisation by electron microscopy and the effects of isolated αC fragments on polymerization. J Biol Chem. 268:1993;13577-13585.
138. GORKUN O.V., VEKLICH Y.I., MEDVED L.V., HENSCHEN A.H., WEISEL J.W. Role of alpha C domains of fibrin in clot formation. Biochemistry. 33:1994;6986-6998.
139. HESSEL, B., BLOMBÄCK, B. and SÖDERMAN, S. Fibrin formation in presence of trypsin. In: Fibrinogen - Recent Biochemical and Medical Aspects. pp. 101-108. A. Henschen, H. Graeff, F. Lottspeich (eds.), Walter de Gruyter & Co., Berlin-New York 1982.
140. RUDCHENKO S., TRAKHT I., SOBEL J.H. Comparative structure and functional features of the human fibrinogen alpha C domain and the isolated alpha C fragment. Characterization using monoclonal antibodies to defined COOH-terminal A alpha chain regions. J Biol Chem. 271:1996;2523-2530.
141. WEISEL J.W., PAPSUN D.M. Involvement of the COOH-terminal portion of the alpha-chain of fibrin in the branching of fibers to form a clot. Thromb Res. 47:1987;155-163.
142. KUDRYK B., BINI A., PROCYK R., MATSUEDA G.R., SHAINOFF J.R. Cross-linking of fibrinogen by tissue transglutaminase: Involvement of the C-termini of the Aα- and γ-chain in formation of Aαγ-dyads. Thromb Haemost. 69:1993;2560. Abs.
143. BLOMBÄCK, B., ADAMSON, L., HESSEL, B., HOLMGREN, A., HOGG, D. and PROCYK, R. The effect of thioredoxin system and thiols on some coaguloproteins. In: Thioredoxin and Glutaredoxin Systems; Structure and Function. A. Holmgren, C.-I. Brändén, H. Jörnvall and B.-M. Sjöberg (eds.), pp. 357-367, Raven Press, New York 1986.
144. ZHANG J.-Z., REDMAN C.M. Identification of Bβ chain domains involved in human fibrinogen assembly. J Biol Chem. 267:1992;21727-21732.
145. ZHANG J.-Z., KUDRYK B., REDMAN C.M. Symmetrical disulfide bonds are not necessary for assembly and secretion of human fibrinogen. J Biol Chem. 268:1993;11278-11282.
146. LOEWY A.G. Some thoughts on the state in nature, biosynthetic origin and function of factor XIII. Ann NY Acad Sci. 202:1972;41-58.
147. LORAND L. Fibrinoligase: the fibrin-stabilizing factor system of blood plasma. Ann NY Acad Sci. 202:1972;6-30.
148. DOOLITTLE R.F., CASSMAN K.G., CHEN R., SHARP J.J., WOODING G.L. Correlation of the mode of fibrin polymerization with pattern of cross-linking. Ann NY Acad Sci. 202:1972;114-126.
149. McKEE P.A., SCHWARTZ M.L., PIZZO S.V., HILL R.L. Cross-linking of fibrin by fibrin-stabilizing factor. Ann NY Acad Sci. 202:1972;127-148.
150. PISANO J.J., BRONZERT T.J., PEYTON M.P., FINLAYSON J.S. ε (γ-glutamyl) lysine cross-links: Determination in fibrin from normal and factor XIII-deficient individuals. Ann NY Acad Sci. 202:1972;98-113.
151. SIEBENLIST K.R., MEH D.A., WALL J.S., HAINFELD J.F., MOSESSON M.W. Orientation of the carboxy-terminal regions of fibrin γ chain dimers determined from the crosslinked products formed in mixtures of fibrin, fragment D and factor XIIIa. Thromb Haemost. 74:1995;1113-1119.
152. MOSESSON M.W., SIEBENLIST K.R., AMRANI D.L., DiORIO J.P. Identification of covalently linked trimeric and tetrameric D domains in crosslinked fibrin. Proc Natl Acad Sci USA. 86:1989;1113-1117.
153. SIEBENLIST K.R., MOSESSON M.W. Factors affecting γ-chain multimer formation in cross-linked fibrin. Biochemistry. 31:1992;936-941.
154. KANAIDE H., SHAINOFF J.R. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J Lab Clin Med. 85:1975;574-597.
155. COTTRELL B.A., STRONG D.D., WATT K.V., DOOLITTLE R.F. Amino acid sequence studies on the α chain of human fibrinogen. Exact location of cross-linking acceptor sites. Biochemistry. 18:1979;5405-5410.
156. LY B., KIERULF P., JAKOBSEN E. Stabilization of soluble fibrin/fibrinogen complexes by fibrin stabilizing factor (FSF). Thromb Res. 4:1974;509-522.
157. SOBEL J.H., THIBODEAU C.A., CANFIELD R.E. Early alpha chain cross-linking in human fibrin preparations. Thromb Haemost. 60:1988;153-159.
158. SHAINOFF J.R., URBANIC D.A., DiBELLO P.M. Immunoelectrophoretic characterization of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. Identification of a rapid mode of hybrid alpha-/gamma-chain cross-linking that is promoted by the gamma-chain cross-linking. J Biol Chem. 266:1991;6429-6437.
159. MURTHY S.N., WILSON J., GUY S.L., LORAND L. Intramolecular cross-linking of monomeric fibrinogen by tissue transglutaminase. Proc Natl Acad Sci USA. 88:1991;10601-10604.
160. GRØN B., FILION-MYKLEBUST C., BENNICK A., NIEUWENHUIZEN W., MATSUEDA G.R., BROSSTAD F. Early cross-linked fibrin in human plasma contains α-polymers with intact fibrinopeptide A. Blood Coagul Fibrinol. 3:1992;731-736.
161. s-γt-chain hybrids in plasma clots studied by 1D and 2D electrophoresis and Western blotting. Thromb Haemost. 70:1993;438-442.
162. KRAKOW W., ENDRES G.F., SIEGEL B.M., SCHERAGA H.A. An electron microscopic investigation of the polymerization of bovine fibrin monomer. J Mol Biol. 71:1972;95-103.
163. WILLIAMS R.C. Morphology of fibrinogen monomers and fibrin protofibrils. Ann NY Acad Sci. 408:1983;180-193.
164. HANTGAN R.R., HERMANS J. Assembly of fibrin. A light scattering study. J Biol Chem. 254:1979;11272-11281.
165. PORTER K.R., HAWN C.v.Z. Sequences in the formation of clots from purified bovine fibrinogen and thrombin: A study with the electron microscope. J Exp Med. 90:1949;225-232.
166. SHAH G.A., FERGUSON I.A., DHALL T.Z., DHALL D.P. Polydispersion in the diameter of fibres in fibrin networks: Consequences on the measurement of mass-length ratio by permeability and turbidity. Biopolymers. 21:1982;1037-1047.
167. MÜLLER M.F., RIS H., FERRY J.D. Electron microscopy of fine fibrin clots and fine and coarse fibrin films. Observations of fibers in cross-section and in deformed states. J Mol Biol. 174:1984;369-384.
168. MOSESSON M.W., DiORIO J.P., MÜLLER M.F., SHAINOFF J.R., SIEBENLIST K.R., AMRANI D.L., HOMANDBERG G.A., SORIA J., SORIA C., SAMAMA M. Studies on the ultra structure of fibrin lacking fibrinopeptide B (β-fibrin). Blood. 69:1987;1073-1081.
169. FERRY J.D., MORRISON P.R. Preparation and properties of serum and plasma proteins VIII. The conversion of human fibrinogen to fibrin under various conditions. J Am Chem Soc. 69:1947;388-400.
170. CARR M.E. JR., HERMANS J. Size and density of fibrin fibers from turbidity. Macromolecules. 11:1978;46-50.
171. CARR M.E., GABRIEL D.A. Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity. Macromolecules. 13:1980;1473-1477.
172. BLOMBÄCK B., CARLSSON K., HESSEL B., LILJEBORG A., PROCYK R., ÅSLUND N. Native fibrin gel networks observed by 3D microscopy, permeation and turbidity. Biochim Biophys Acta. 997:1989;96-110.
173. OKADA, M., BLOMBÄCK, B. and BLOCK, M. Effect of albumin and dextran on fibrin gel structure. Thromb Haemost 50, 613 Abs., p. 201, 1983.
174. WAUGH D.F. Protein-protein interactions. Advan Protein Chem. 9:1954;325-437.
175. LAURENT T.C. An early look at macromolecular crowding. Biophys Chem. 57:1995;7-14.
176. MARX G. Elasticity of fibrin and protofibrin gels is differentially modulated by calcium and zinc. Thromb Haemost. 59:1988;500-503.
177. OKADA M., BLOMBÄCK B., CHANG MING-DER, HOROWITZ B. Fibronectin and fibrin gel structure. J Biol Chem. 260:1985;1811-1820.
178. ROBERTS W.W., KRAMER O., ROSSER R.W., NESTLER F.H.M., FERRY J.D. Rheology of fibrin clots. I. Dynamic viscoelastic properties and fluid permeation Biophys Chem. 1:1974;152-160.
179. CARR M.E., SHEN L.L., HERMANS J. A physical standard of fibrinogen: Measurement of the elastic modulus of dilute fibrin gels with a new elastometer. Analyt Biochem. 72:1976;202-211.
180. SHEN L.L., HERMANS J., McDONAGH J., McDONAGH R.P. Role of fibrinopeptide B release: comparison of fibrins produced by thrombin and Ancrod. Am J Physiol. 232:1977;H629-H633.
181. SHEN L.L., McDONAGH R.P., McDONAGH J., HERMANS J. Early events in the plasmin digestion of fibrinogen and fibrin. Effects of plasmin on fibrin polymerization. J Biol Chem. 252:1977;6184-6189.
182. SHAH G.A., NAIR C.H., DHALL D.P. Comparison of fibrin networks in plasma and fibrinogen solution. Thromb Res. 45:1987;257-264.
183. LARSSON U., BLOMBÄCK B., RIEGLER R. Fibrinogen and the early stages of polymerization to fibrin as studied by dynamic laser light scattering. Biochim Biophys Acta. 915:1987;172-179.
184. BACH-GANSMO E.T., HALVORSEN S., GODAL H.C., SKJØNSBERG O.H. Degradation of the α-chain of fibrin by human neutrophil elastase reduces the stimulating effect of fibrin on plasminogen activation. Thromb Res. 75:1994;307-317.
185. BINI A., CALLENDER S., PROCYK R., BLOMBÄCK B., KUDRYK B.J. Flow and antibody binding properties of hydrated fibrins prepared from plasma, platelet rich plasma and whole blood. Thromb Res. 76:1994;145-156.
186. MARX G. Modeling cation-driven (proto)fibrin coagulation. Biopolymers. 29:1990;1233-1241.
187. HUNZIKER E.B., STRAUB P.W., HAEBERLI A. A new concept of fibrin formation based upon the linear growth of interlacing and branching polymers and molecular alignment into interlocked single-stranded segments. J Biol Chem. 265:1990;7455-7463.
188. MEGA, J.I. SHAINOFF, J.R. and DRESHAR, D.A. Dissociation of α-fibrin at elevated temperatures. In: Fibrinogen 3. Biochemistry, Biological Functions, Gene Regulation and Expression. M.W. Mosesson, D.L. Amrani, K.R. Siebenlist and J.P. DiOrio (eds.), pp. 83-86. Elsevier Science, Amsterdam 1988.
189. BECKER C.M. Bovine fibrinogen aggregates: Electron microscopic observations of quasi-globular structures. Thromb Res. 48:1987;101-110.
190. BROSSTAD F., KIERULF P., GODAL H.C. The fibrin-solubilizing effect of fibrinogen as studied by light scattering. Thromb Res. 14:1979;705-712.
191. MIHALYI E. Kinetics and molecular mechanism of the proteolytic fragmentation of fibrinogen. Ann NY Acad Sci. 408:1983;60-70.
192. NUSSENZWEIG V., SELIGMANN M., PELMONT J., GRABAR P. Les produits de degradation du fibrinogéne humain par la plasmine. I. Separation et propriétés physico-chemiques Ann Inst Pasteur. 100:1961;377-388.
193. MARDER V.J., SHULMAN N.R., CARROLL W.R. High molecular weight derivatives of human fibrinogen produced by plasmin. I. Physicochemical and immunological characterization J Biol Chem. 244:1969;2111-2119.
194. NY T., PENG X.-R., OHLSSON M. Hormonal regulation of the fibrinolytic components in the ovary. Thromb Res. 71:1993;1-45.
195. WALLÉN, P. Biochemistry of plasminogen. In: Fibrinolysis. D. Kline and K.N.N. Reddy (eds.), pp. 1-24, CRC Press, Boca Raton, FL 1980.
196. THORSEN S. Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation influence of ω-aminocarboxylic acids. Biochim Biophys Acta. 393:1975;55-65.
197. CEDERHOLM-WILLIAMS S.A. The binding of plasminogen (Mol. WT. 84,000) and plasmin to fibrin. Thromb Res. 11:1977;421-423.
198. ADAMS LUCAS M., FRETTO L.J., McKEE P.A. The binding of human plasminogen to fibrin and fibrinogen. J Biol Chem. 258:1983;4249-4256.
199. DE SERRANO V.S., URANO T., GAFFNEY P.J., CASTELLINO F.J. Influence of vaious structural domains of fibrinogen and fibrin on the poentiation of plasminogen activation by recombinant tissue plasminogen activator. J Prot Chem. 8:1989;61-77.
200. SOTTRUP-JENSEN, L., CLAEYS, H., ZAJDEL, M., PETERSEN, T.E. and MAGNUSSON, S. Progress in Chemical Fibrinlysis. vol. 3. J.F. Davidson, R.M. Rowan, M.M. Samama and P.C. Desnayers (eds.), pp. 191-209, Raven Press, New York 1978.
201. SUENSON E., LÜTZEN O., THORSEN S. Initial plasmin-degradation of fibrin as the basis of a positive feed-back mechanism in fibrinolysis. Eur J Biochem. 140:1984;513-522.
202. TRAN-THANG C., KRUITHOF E.K., BACHMANN F. Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots. J Clin Invest. 74:1984;2009-2016.
203. TRAN-THANG C., KRUITHOF E.K.O., ATKINSON J., BACHMAN F. High affinity binding sites for human Glu-plasminogen unveiled by limited plasmic degradation of human fibrin. Eur J Biochem. 160:1986;599-604.
204. SUENSON E., BJERRUM P., HOLM A., LIND B., MELDAL M., SELMER J., PETERSEN L.C. The role of fragment X polymers in the fibrin enhancement of tissue plasminogen activator-catalyzed plasmin formation. J Biol Chem. 265:1990;22228-22237.
205. GARMAN A.J., SMITH R.A.G. The binding of plasminogen to fibrin: Evidence of plasminogen-bridging. Thromb Res. 27:1982;311-320.
206. WEISEL J.W., NAGASWAMI C., KORSHOLM B., PETERSEN L.C., SUENSON E. Interactions of plasminogen with polymerizing fibrin and its derivatives, monitored with a photoaffinity cross-linker and electron microscopy. J Mol Biol. 235:1994;1117-1135.
207. ASTRUP T., PERMIN P.M. Fibrinolysis in the organism. Nature. 159:1947;681-683.
208. COLE E.R., BACHMAN F.W. Purification and properties of a plasminogen activator from pig heart. J Biol Chem. 252:1977;3729-3737.
209. RIJKEN D.C., WIJNGAARDS G., ZAAL-DE JONG M., WELBERGEN J. Purification and partial characterization of plasminogen activator from human uterine tissue. Biochim Biophys Acta. 580:1979;140-153.
210. WALLÉN, P., RÅNBY, M., BERGSDORF, N. and KOK, P. Purification and characterization of tissue plasminogen activator: On the occurrence of two different forms and their enzymatic properties. In: Progress in Fibrinolysis. vol. 5. J.F. Davidson, I.M. Nilsson, and B. Åstedt (eds.), pp. 16-23, Churchill Livingstone, Edinburgh 1981.
211. WALLÉN P., BERGSDORF N., RÅNBY M. Purification and identification of two structural variants of porcine tissue plasminogen activator by affinity adsorption on fibrin. Biochim Biophys Acta. 719:1982;318-328.
212. PENNICA D., HOLMES W.E., KOHR W.J., HARKINS R.N., VEHAR G.A., WARD C.A., BENNETT W.F., YELVERTON E., SEEBURG P.H., HEYNEKER H.L, GOEDDEL D.V., COLLEN D. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature. 301:1983;214-221.
213. WALLÉN P., POHL G., BERGSDORF N., RÅNBY M., NY T., JÖRNVALL H. Purification and characterization of a melanoma cell plasminogen activator. Eur J Biochem. 132:1983;681-686.
214. CHENG X.-F., BROHLIN M., POHL G., BÄCK O., WALLÉN P. Binding of tissue plasminogen activator to endothelial cells. Thromb Res. 77:1995;149-164.
215. JÖRNVALL H., POHL G., BERGSDORF N., WALLÉN P. Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity. FEBS Lett. 156:1983;47-50.
216. CAMIOLO S.M., THORSEN S., ASTRUP T. Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase-activated human globulin, and plasmin. Proc Soc Exp Biol Med. 138:1971;277-280.
217. THORSEN S., GLAS-GREENWALT P., ASTRUP T. Differences in the binding to fibrin of urokinase and tissue plasminogen activator. Thromb Diath Haemorrh. 28:1972;65-74.
218. WALLÉN, P. and WIMAN, B. Purification of tissue activator using affinity adsorption on fibrin and hydrophobic interaction chromatography. Effect of fibrin on the enzymatic properties of the activator. 5th Congress on Thrombosis and Haemostasis. Int. Soc. Thrombosis and Haemostasis. Paris, 1975: p. 348, Abs. 331.
219. WALLÉN, P. Activation of plasminogen with urokinase and tissue activator. In: Thrombosis and Urokinase. P. Paoletti and S. Sherry (eds.), pp. 91-102, Academic Press, London, New York, San Francisco 1977.
220. SUENSON E., PETERSEN L.C. Fibrin and plasminogen structures essential to stimulation of plasmin formation by tissue-type plasminogen activator. Biochim Biophys Acta. 870:1986;510-519.
221. HALVORSEN S., SKJØNSBERG O.H., GODAL H.C. The stimulatory capacity of soluble fibrin prepared from high and low molecular weight fibrinogen on plasminogen activation. Blood Coagul Fibrinol. 4:1993;133-137.
222. SORIA, J., SORIA, C., BERTRAND, O., MIRHSAKI, M., DUNN, R.W., SUENSON, E., DESVIGNES, P., BONNET, P., SAMAMA, M. and CAEN, J.P. Role of fibrin polymerization in fibrinolysis: Comparison between polymerizable and unpolymerizable fibrins in the potentiating effect of plasminogen activation by tissue-type plasminogen activator (t-PA). In: Fibrinogen-Fibrin Formation and Fibrinolysis. Vol. 4. D. Lane, A. Henschen and M.K. Jasani (eds.), pp. 153-158. Walter de Gruyter & Co, Berlin-New York 1986.
223. NORRMAN B., POHL G., JÖRNVALL H., WALLÉN P. Proteolytically induced variations in the enzymatic properties of tissue plasminogen activator. Activations, inactivations and reactivations. Eur J Biochem. 159:1986;7-13.
224. NORRMAN B., WALLÉN P., RÅNBY M. Fibrinolysis mediated by tissue plasminogen activator. Disclosure of a kinetic transition. Eur J Biochem. 149:1985;193-200.
225. FLEURY V., ANGLÉS-CANO E. Characterization of the binding of plasminogen to fibrin surfaces: The role of carboxy-terminal lysines. Biochemistry. 30:1991;7630-7638.
226. SCHIELEN W.J.G., VOSKUILEN M., TESSER G.I., NIEUWENHUIZEN W. The sequence Aα-(148-160) in fibrin, but not in fibrinogen, is accessible to monoclonal antibodies. Proc Natl Acad Sci USA. 86:1989;8951-8954.
227. 152Val of the fibrinogen Aα chain in the fibrin-induced rate enhancement of the plasminogen activation by t-PA. Fibrinolysis. 7:1993;63-67.
228. YONEKAWA O., VOSKUILEN M., NIEUWENHUIZEN W. Localization in the fibrinogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasminogen activator-catalyzed activation of plasminogen. Biochem J. 283:1992;187-191.
229. HADDELAND U., SLETTEN K., BENNICK A., NIEUWENHUIZEN W., BROSSTAD F. Aggregated, conformationally changed fibrinogen exposes the stimulating sites for t-PA-catalyzed plasminogen activation. Thromb Haemost. 75:1996;326-331.
230. HADDELAND U., SLETTEN K., BENNICK A., BROSSTAD F. Freeze-dried fibrinogen or fibrinogen in EDTA stimulate the tissue plasminogen activator - catalyzed conversion of plasminogen to plasmin. Blood Coag Fibrinol. 5:1994;575-581.
231. RADCLIFFE R., HEINZE T. Stimulation of tissue plasminogen activator by denatured proteins and fibrin clots: A possible additional role for plasminogen activator? Arch Biochem Biophys. 211:1981;750-761.
232. SOEDA S., SHIMENO H., NAGAMATSU A. A comparison of bovine serum albumins, modified with a variety of carboxyl group agents, as stimulators of tissue-type plasminogen activator catalyzed activation of plasminogen. Chem Pharmacol Bull. 37:1989;723-728.
233. CHMIELEWSKA J., RÅNBY M., WIMAN B. Evidence for a rapid inhibitor to tissue plasminogen activator in plasma. Thromb Res. 31:1983;427-436.
234. YAMAMOTO C., KAJI T., SAKAMOTO M., KOZUKA H., KOIZUMI F. Calcium regulation of plasminogen activator and plasminogen activator inhibitor-1 release from cultured human vascular endothelial cells. Thromb Res. 74:1994;163-168.
235. LIU C.Y., WALLÉN P., HANDLEY A. Preparation of active iodinated and gold labeled tissue plasminogen activator and its binding to fibrin and endothelial cells. Thromb Haemost. 54:1985;60.
236. HAJJAR K.A., HAMEL N.M., HARPEL P.C., NACHMAN R.L. Binding of tissue plasminogen activator to cultured human endothelial cells. J Clin Invest. 80:1987;1712-1719.
237. CHENG X.-F., BÄCK O., NILSSON T.K., NYLANDER-LUNDQUIST E., POHL G., WALLÉN P. Binding of tissue plasminogen activator to human endothelial cells. Importance of the B-chain as ligand. Biochem J. 287:1992;407-413.
238. HAJJAR, K.A. and JACOVINA, A.T. Molecular cloning of an endothelial cell tissue plasminogen activator/plasminogen receptor: Annexin II-related protein. Thromb Haemost 69, 1601 Abs., p. 989, 1993.
239. SOBERANO M.E., ONG E.B., JOHNSON A.J., LEVY M., SCHOELLMANN G. Purification and characterization of two forms of urokinase. Biochim Biophys Acta. 445:1976;763-773.
240. STUMP D.C., LIJNEN H.R., COLLEN D. Purification and characterization of single-chain urokinase-type plasminogen activator from human cell cultures. J Biol Chem. 261:1986;1274-1278.
241. COLLEN D., STASSEN J.M., BLABER M., WINKLER M., VERSTRAETE M. Biological and thrombolytic properties of proenzyme and active forms of human urokinase-III. Thrombolytic properties of natural and recombinant urokinase in rabbits with experimental jugular vein thrombosis. Thromb Haemost. 52:1984;27-30.
242. GUREWICH V., PANNELL R., LOUIE S., KELLEY P., SUDDITH R.L., GREENLEE R. Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urolinase): A study in vitro and in two animal species. J Clin Invest. 73:1984;1731-1739.
243. LOEWY A.G., SANTER U.V., WIECZOREK M., BLODGETT J.K., JONES S.W., CHERONIS J.C. Purification and characterization of a novel zinc-proteinase from cultures of Aeromonas hydrophila. J Biol Chem. 268:1993;9071-9078.
244. PANNELL R., GUREVICH V. Pro-urokinase: a study of its stability in plasma and of a mechanism for its selective fibrinolytic effect. Blood. 67:1986;1215-1223.
245. PLOW E.F. Leukocyte elastase release during blood coagulation. A potential mechanism for activation of the alternative fibrinolytic pathway. J Clin Invest. 69:1982;564-572.
246. BACH-GANSMO E.T., HALVORSEN S., GODAL H.C., SKJØNSBERG O.H. Impaired clot lysis in the presence of human neutrophil elastase. Thromb Res. 80:1995;153-159.
247. YAMAMOTO J., ISHII I., OKADA Y., YAMASHITA T., RIDLER C.D., GOROG P., KOVACS I.B. Effect of leucocyte products on platelet thrombus formation, coagulation and spontaneous thrombolysis, as measured from native human blood, in vitro. Thromb Res. 71:1993;281-287.
248. BINI A., ITOH Y., KUDRYK B.J., NAGASE H. Degradation of cross-linked fibrin by matrix metalloproteinase 3 (Stromelysin 1): Hydrolysis of γGLY404-ALA405 peptide bond. Circulation. 92:1995;2986.
249. RETZIOS A.D., MARKLAND F.S. Fibrinolytic enzymes from the venoms of Agkistrodon contortrix contortrix and Crotalus basilicus basilicus: Cleavage site specificity towards the α-chain of fibrin. Thromb Res. 74:1994;355-367.
250. ROBBINS, K.C. and MARKUS, G. The interaction of human plasminogen with streptokinase. In: Fibrinolysis. P.J. Gaffney and S. Balkuv-Ulutin (eds.), pp. 61-75. Academic Press, London, New York, San Francisco 1978.
251. TAKADA A., MOCHIZUKI K., TAKADA Y. Further characterization of SK-potentiators of plasminogen. Thromb Res. 19:1980;485-492.
252. TAKADA A., TAKADA Y., SUGAWARA Y. The activation of Glu- and Lysplasminogen by streptokinase: Effects of fibrin, fibrinogen and their degradation products. Thromb Res. 37:1985;465-475.
253. HISHIKAWA-ITOH Y., SUGIE I., KATO H., IWANAGA S. Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: Its identification as a fibrinogen degradation product. J Biochem. 92:1982;1129-1140.
254. MATSUO O., OKADA K., FUKAO H., TOMIOKA Y., UESHIMA S., WATANUKI M., SAKAI M. Thrombolytic properties of staphylokinase. Blood. 76:1990;925-929.
255. 2-plasmin inhibitor on plasminogen activation by staphylokinase/plasminogen complex. Thromb Res. 76:1994;211-220.
256. 2-antiplasmin and fibrin. Biochim Biophys Acta. 1118:1992;144-148.
257. 2-antiplasmin and fibrin of the activation of plasminogen with recombinant staphylokinase in plasma. Blood. 82:1993;1175-1183.
258. HESSEL B. On the structure of the COOH-terminal part of the A α chain of human fibrinogen. Thromb Res. 7:1975;75-87.
259. 3 (platelet GPIIb-IIIa). Cell. 65:1991;409-416.
260. SAKHAROV D.V., RIJKEN D.C. Superficial accumulation of plasminogen during plasma clot lysis. Circulation. 92:1995;1883-1890.
261. SAKHAROV D.V., NAGELKERKE J.F., RIJKEN D. Rearrangements of the fibrin network and spatial distribution of fibrinolytic components during plasma clot lysis. J Biol Chem. 271:1996;2133-2138.
262. THOMPSON W.D., CAMPBELL R., EVANS A.T. Fibrin degradation and angiogenesis: Quantitative analysis of the angiogenic response in the chick chorioallantoic membrane. J Pathol. 145:1985;27-37.
263. THOMPSON W.D., SMITH E.B., STIRK C.M., MARSHALL F.I., STOUT A.J., KOCCHAR A. Angiogenic activity of fibrin degradation products is located in fibrin fragment E. J Pathol. 168:1992;47-53.
264. SMITH E.B., THOMPSON W.D. Fibrin as a factor in atherogenesis. Thromb Res. 73:1994;1-19.
265. KERN D.F., SALDEEN K., SALDEEN T., MALIK A.B. Pulmonary vascular effects of a fibrin(ogen)-derived vasoactive peptide. Thromb Res. 42:1986;783-788.
266. NICHOLS W.W., MEHTA J., WARGOVICH T., SALDEEN K., WALLIN R., SALDEEN T. Fibrin(ogen)-derived peptide Bβ30-43 increases coronary blood flow in the anesthetized dogs. Thromb Res. 38:1985;223-229.
267. SALDEEN K., NICHOLS W., LAWSON D., ANDERSSON R., SALDEEN T., MEHTA J. Fibrin(ogen) degradation product peptide 6A increases femoral artery blood flow in dogs. Acta Physiol Scand. 142:1991;339-344.
268. BOUTCHER P.A., GAFFNEY P.J., RAUT S., O'REGAN R.G., McLUGHLIN P. Effects of early plasmin digests of fibrinogen on isometric tension development in isolated rings of rat pulmonary artery. Thromb Res. 81:1996;231-239.
269. OUIMET, H. and LOSCALZO, J. Fibrinolysis. In: Thrombosis and Haemorrhage. J. Loscalzo and J.A. Shafer (eds.), pp. 127-143, Blackwell Sci Publ, London 1994.
270. 2-antiplasmin inhibitor from human plasma. J Biol Chem. 251:1976;5956-5965.
271. COLLEN D. Identification and some properties of a new fast reacting plasmin inhibitor in plasma. Eur J Biochem. 69:1976;209-216.
272. WIMAN B., COLLEN D. Molecular mechanism of physiological fibrinolysis. Nature. 272:1978;549-550.
273. 2-antiplasmin inhibitor from plasma fibrin clots by activated coagulation factor XIII. Its effect on fibrinolysis. J Clin Invest. 77:1986;1006-1013.
274. 2-antiplasmin inhibitor. J Biol Chem. 261:1986;15591-15595.
275. 2-antiplasmin to fibrin is a key factor in regulating blood clot lysis: species differences. Blood Coagul Fibrinol. 4:1993;869-875.
276. 2-antiplasmin by platelets. Thromb Haemost. 75:1996;161-167.
277. OKAMOTO S., OKAMOTO U. Amino-methyl-cyclohexane-carboxylic acid: AMCHA; A new patent inhibitor of the fibrinolysis. Keio J Med. 11:1962;105-115.
278. KRISHNAMURTI C., VUKELJA S.J., ALVING B.M. Inhibitory effects of lysine analogues on t-PA induced whole blood clot lysis. Thromb Res. 73:1994;419-430.
279. WANAKA K., OKAMOTO S., HORIE N., HIJAKA-OKUNOMIYA A.K., OKAMOTO U., NAITO T., OHNO N., BOHGAKI M., TSUDA Y., OKADA Y. Use of an active center-directed plasmin inhibitor elucidates the multiplicity of plasmin actions. Thromb Res. 82:1996;79-86.
280. McLEAN J.W., TOMLINSON J.E., KUANG W.-J., EATON D.L., CHEN E.Y., FLESS G.M., SCANU A.M., LAWN R.M. cDNA sequence of human apolipoprotein(a) is homologous to plasminogen. Nature. 330:1987;132-137.
281. HARPEL P.C., GORDON B.R., PARKER T.S. Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin. Proc Natl Acad Sci USA. 86:1989;3847-3851.
282. ROUY D., GRAILHE P., NIGON F., CHAPMAN J., ANGLÉS-CANO E. Lipoprotein(a) impairs generation of plasmin by fibrin-bound tissue-type plasminogen activator. In vitro studies in a plasma milieu. Arteroscler Thromb. 11:1991;629-638.
283. ROUY D., KOSCHINSKY M.L., FLEURY V., CHAPMAN J., ANGLÉS-CANO E. Apolipoprotein(a) and plasminogen interactions with fibrin: A study with recombinant apolipoprotein(a) and isolated plasminogen fragments. Biochemistry. 31:1992;6333-6339.
284. EDELBERG J.M., GONZALEZ-GRONOW M., PIZZO S.V. Lipoprotein(a) inhibition of plasminogen activation by tissue-type plasminogen activator. Thromb Res. 57:1990;155-162.
285. LOSCALZO J., WEINFELD M., FLESS G.M., SCANU A.M. Lipoprotein(a), fibrin binding, and plasminogen activation. Arterioscler. 10:1990;240-245.
286. AZNAR J., ESTELLÉS A., BRETÓ M., ESPANA F. Euglobulin clot lysis induced by tissue type plasminogen activator in subjects with increased levels and different isoforms of lipoprotein (a). Thromb Res. 72:1993;459-465.
287. GODAL H.C. The effect of EDTA on human fibrinogen and its significance for the coagulation of fibrinogen with thrombin. Scand J Clin Lab Invest. 12(Suppl. 53):1960;1-20.
288. BLOMBÄCK B., BLOMBÄCK M., LAURENT T.C., PERTOFT H. Effect of EDTA on fibrinogen. Biochim Biophys Acta. 127:1966;560-562.
289. LY B., GODAL H.C. Thrombin clotting time - A more sensitive indicator of denatured fibrinogen than clottability. Haemostasis. 1:1972;44-51.
290. HAVERKATE F., TIMAN G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. Thromb Res. 10:1977;803-812.
291. MARGUERIE G., CHAGNIEL G., SUSCILLON M. The binding of calcium to bovine fibrinogen. Biochim Biophys Acta. 490:1977;94-103.
292. NIEUWENHUIZEN W., VAN RUIJVEN-VERMEER I.A.M., NOOIJEN W.J., VERMOND A., HAVERKATE F., HERMANS J. Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation products. Thromb Res. 22:1981;653-657.
293. NIEUWENHUIZEN W., VERMOND A., HERMANS J. Evidence for the localization of a calcium-binding site in the amino-terminal disulphide knot of fibrin(ogen). Thromb Res. 31:1983;81-86.
294. HÖRMANN, H. Interaction with fibrinogen and fibrin. In: Plasma Fibronectin, Structure and Function, vol. 5. J. McDonagh (ed.), pp. 99-120, Marcel Dekker Inc., New York, Basel 1985.
295. MOSHER D.F. Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem. 250:1975;6614-6621.
296. 2-macroglobulin in clotting plasma. J Biol Chem. 251:1976;1639-1645.
297. IWANAGA S., SUZUKI K., HASHIMOTO S. Bovine plasma cold-insoluble globulin: Gross structure and function. Ann NY Acad Sci. 312:1978;56-73.
298. McDONAGH R.P., McDONAGH J., PETERSEN T.E., THØGERSEN H.C., SKORSTENGAARD K., SOTTRUP-JENSEN L., MAGNUSSON S. Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin. FEBS Lett. 127:1981;174-178.
299. EHRLICH P.H., SOBEL J.H., MOUSTAFA Z.A., CANFIELD R.E. Monoclonal antibodies to α-chain regions of human fibrinogen that participate in polymer formation. Biochemistry. 22:1983;4184-4192.
300. PROCYK R., BISHOP P.D., KUDRYK B. Fibrin-recombinant human factor XIII. A subunit association. Thromb Res. 71:1993;127-138.
301. HORNYAK T.J., SHAFER J.A. Interactions of factor XIII with fibrin as substrate and cofactor. Biochemistry. 31:1992;423-429.
302. GREENBERG C.S., SHUMAN M.A. The zymogen forms of blood coagulation factor XIII bind specifically to fibrinogen. J Biol Chem. 257:1982;6096-6101.
303. MARY A., ACHYUTHAN K.E., GREENBERG C.S. Factor XIII binds to the Aα- and Bβ-chains in the D-domain of fibrinogen: An immunoblotting study. Biochem Biophys Res Commun. 147:1987;608-614.
304. FUKUE H., ANDERSON K., McPHEDRAN P., CLYNE L., McDONAGH J. A unique factor XIII inhibitor to a fibrin-binding site on factor XIIIa. Blood. 79:1992;65-74.
305. PEDERSEN L.C., YEE V.C., BISHOP P.D., Le TRONG I., TELLER D.C., STENKAMP R.E. Transglutaminase factor XIII uses proteinase-like catalytic triad to cross link macromolecules. Protein Sci. 3:1994;1131-1135.
306. MICANOVIC R., PROCYK R., LIN W., MATSUEDA G.R. Role of histidine 373 in the catalytic activity of coagulation factor XIII. J Biol Chem. 269:1994;9190-9194.
307. YEE V.C., PEDERSEN L.C., Le TRONG I., BISHOP P.D., STENKAMP R.E., TELLER D.C. Three-dimensional structure of a transglutaminase: Human blood coagulation factor XIII. Proc Natl Acad Sci USA. 91:1994;7296-7300.
308. LORAND L., CREDO R.B., JANUS T.J. Factor XIII (Fibrin stabilizing factor). Methods Enzymol. 80C:1981;333-341.
309. DE BACKER-ROYER C., MEUNIER J.C. Effect of temperature and pH on factor XIIIa from human placenta. Int J Biochem. 24:1992;637-642.
310. +2-related regulatory function of fibrinogen. Proc Natl Acad Sci USA. 75:1978;4234-4237.
311. BULUK K., JANUSZKA T., OLBRAMSKI J. Conversion of fibrin to desmofibrin. Nature. 191:1961;1093-1094.
312. GREENBERG C.S., ACHYUTAN K.E., FENTON J.W. II Factor XIIIa formation promoted by complexing of α-thrombin, fibrin and plasma factor XIII. Blood. 69:1987;867-871.
313. GREENBERG C.S., ACHYUTHAN K.E., RAJAGOPALAN S., PIZZO S.V. Characterization of the fibrin polymer structure that accelerates thrombin cleavage of plasma factor XIII. Arch Biochem Biophys. 262:1988;142-148.
314. NASKI M.C., LORAND L., SHAFER J.A. Characterization of the kinetic pathway for fibrin promotion of α-thrombin-catalyzed activation of plasma factor XIII. Biochemistry. 30:1991;934-941.
315. CREDO R.B., CURTIS C.G., LORAND L. Alpha-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects. Biochemistry. 20:1981;3770-3778.
316. YEE V.C., PEDERSEN L.C., BISHOP P.D., STENKAMP R.E., TELLER D.C. Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res. 78:1995;389-397.
317. HAWIGER J. Adhesive interactions of platelets and their blockade. Ann NY Acad Sci. 614:1991;270-278.
318. PEERSCHKE E.B. The platelet fibrinogen receptor. Semin Hematol. XXII:1985;241-259.
319. VU T.-K.H., HUNG D.T., WHEATON V.I., COUGHLIN S.R. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 64:1991;1057-1068.
320. 2+ mobilization. FEBS Lett. 288:1991;123-128.
321. STORCK J., KÜSTERS B., ZIMMERMANN E.R. The tethered ligand receptor is the responsible receptor for the thrombin induced release of von Willebrand factor from endothelial cells (HUVEC). Thromb Res. 77:1995;249-258.
322. DERIAN C.K., SANTULLI R.J., TOMKO K.A., HAERTLEIN B.J., ANDRADE-GORDON P. Species differences in platelet responses to thrombin and SFLLRN. Receptor-mediated calcium mobilization and aggregation, and regulation by protein kinases. Thromb Res. 78:1995;505-519.
323. MUSTARD J.F., PACKHAM M.A., KINLOUGH-RATHBONE R.L., PERRY D.W., REGOECZI E. Fibrinogen and ADP-induced platelet aggregation. Blood. 52:1978;453-466.
324. MARGUERIE G.A., PLOW E.F., EDGINGTON T.S. Human platelets possess an inducible and saturable receptor specific for fibrinogen. J Biol Chem. 254:1979;5357-5363.
325. TOMIKAWA, M., IWAMOTO, M., SÖDERMAN, S. and BLOMBÄCK, B. Effect of fibrinogen on ADP-induced platelet aggregation. Thromb Res 19, 841-855, 1980a.
326. NIEWIAROWSKI S., KORNECKI E., BUDZYNSKI A.Z., MORINELLI T.A., TUSZYNSKI G.P. Fibrinogen interaction with platelet receptors. Ann NY Acad Sci. 408:1983;536-555.
327. COLLER B.S., PEERSCHKE E.I., SCUDDER L.E., SULLIVAN C.A. A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombastenic-like state in normal platelets and binds to glycoproteins IIb and/or IIIa. J Clin Invest. 72:1983;325-338.
328. HAWIGER, J. and TIMMONS, S. Binding of fibrinogen and von Willebrand factor to platelet glycoprotein IIb-IIIa complex. In: Platelets: Receptors, Adhesion, Secretion. Methods in Enzymology. vol. 215 B. J.J. Hawiger (ed.), pp. 228-243, Academic Press, Inc., New York 1992.
329. KLOCZEWIAK M., TIMMONS S., HAWIGER J. Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the γ chain of human fibrinogen and is not involved in the fibrin polymerization reaction. Thromb Res. 29:1983;249-255.
330. KLOCZEWIAK M., TIMMONS S., LUKAS T.J., HAWIGER J. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the γ chain. Biochemistry. 23:1984;1767-1774.
331. KLOCZEWIAK M., TIMMONS S., BEDNAREK M.A., SAKON M., HAWIGER J. Platelet receptor recognition domain on the γ-chain of human fibrinogen and its synthetic peptide analogues. Biochemistry. 28:1989;2915-2919.
332. PLOW E.F., PIERSCHBACHER M.D., RUOSLAHTI E., MARGUERIE G.A., GINSBERG M.H. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci USA. 82:1985;8057-8061.
333. FARRELL D.H., THIAGARAJAN P., CHUNG D.W., DAVIE E.W. Role of fibrinogen α and γ chain sites in platelet aggregation. Proc Natl Acad Sci USA. 89:1992;10729-10732.
334. FARRELL D.H., THIAGARAJAN P. Binding of recombinant fibrinogen mutants to platelets. J Biol Chem. 269:1994;226-231.
335. HARFENIST E.J., PACKHAM M.A., MUSTARD J.F. Effects of the cell adhesion peptide, Arg-Gly-Asp-Ser, on responses of washed platelets from humans, rabbits and rats. Blood. 71:1988;132-136.
336. VERHALLEN, P.F.J. and BARTH, M. Species comparison of anti-aggregatory properties of three fibrinogen receptor-antagonists: RGDS echistatin and the carboxyterminal dodecapeptide of the fibrinogen gamma chain. Thromb Haemost 65, 1613 Abs., p. 1144, 1991.
337. JOLLÈS P., LOUCHEUX-LEFEBVRE M.H., HENSCHEN A. Structural relatedness of κ-casein and fibrinogen γ-chain. J Mol Evol. 11:1978;271-277.
338. JOLLÈS P., LÉVY-TOLEDANO S., FIAT A.-M., SORIA C., GILLESSEN D., THOMAIDIS A., DUNN F.W., CAEN J.P. Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from κ-casein on platelet function. Eur J Biochem. 158:1986;379-382.
339. BAL dit SOLLIER C., DROUET L., PIGNAUD G., CHEVALLIER C., CAEN J., FIAT A.-M., IZQUIERDO C., JOLLÈS P. Effect of κ-casein split peptides on platelet aggregation and on thrombus formation in the guinea-pig. Thromb Res. 81:1996;427-437.
340. CALVETE J.J., ARIAS J., ALVAREZ M.V., LOPEZ M.M., HENSCHEN A., GONZALEZ-RODRIGUEZ J. Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Biochem J. 274:1991;457-463.
341. CALVETE J.J., ARIAS J., ALVAREZ M.V., LOPEZ M.M., HENSCHEN A., GONZALEZ-RODRIGUEZ J. Further studies on the topography of human platelet glycoprotein IIb. Biochem J. 273:1991;767-775.
342. SORIA J., SORIA C., BERTRAND O., SAMAMA M. Fibrinogen and platelet aggregation. Role of the glycopeptidic part and of the fibrinopeptide B. Description of a new technique of fibrinoglycopeptide isolation. Biochem Biophys Res Commun. 82:1978;442-450.
343. STANFORD M.F., MUNOZ P.C., VROMAN L. Platelets adhere where flow has left fibrinogen on glass. Ann NY Acad Sci. 416:1983;504-512.
344. NAGAI H., HANDA M., KAWAI Y., WATANABE K., IKEDA Y. Evidence that plasma fibrinogen and platelet membrane GPIIb-IIIa are involved in the adhesion of platelets to an artificial surface exposed to plasma. Thromb Res. 71:1993;467-477.
345. TOMIKAWA M., IWAMOTO M., OLSSON P., SÖDERMAN S., BLOMBÄCK B. On the platelet-fibrinogen interaction. Thromb Res. 19:1980;869-876.
346. COLLER B.S. Interaction of normal, thrombasthenic and Bernard-Soulier platelets with immobilized fibrinogen: Defective platelet-fibrinogen interaction in thrombastehemia. Blood. 55:1980;169-178.
347. GARTNER T.K., AMRANI D.L., DERRICK J.M., KIRSCHBAUM N.E., MATSUEDA G.R., TAYLOR D.B. Characterization of adhesion of "resting" and stimulated platelets to fibrinogen and its fragments. Thromb Res. 71:1993;47-60.
348. CALVETE J.J., SCHAFER W., MANN K., HENSCHEN A., GONZALEZ-RODRIGUEZ J. Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa. Influence of peptide length. Biochemistry. 206:1992;759-765.
349. D'SOUZA S.E., GINSBERG M.H., BURKE T.A., PLOW E.F. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit. J Biol Chem. 265:1990;3440-3446.
350. D'SOUZA S.E., GINSBERG M.H., MATSUEDA G.R., PLOW E.F. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature. 350:1991;66-68.
351. SHAHBAZI T., JONES N., RADOMSKI M.W., MORO M.A., GINGELL D. Nitric oxide donors inhibit platelet spreading on surfaces coated with fibrinogen but not with fibronectin. Thromb Res. 75:1994;631-642.
352. MENDELSOHN M.E., O'NEILL S., GEORGE D., LOSCALZO J. Inhibition of fibrinogen binding to human platelets by S-nitroso-N-acetylcystine. J Biol Chem. 265:1990;19028-19034.
353. RADOMSKI M.W., REES D.D., DUTRA A., MONCADA S. S-nitroso-glutathione inhibits platelet activation in vitro and in vivo. Br J Pharmacol. 107:1992;745-749.
354. GARTNER T.K., GERRARD J.M., WHITE J.G., WILLIAMS D.C. The endogenous lectin of human platelet is an α-granule component. Blood. 58:1981;153-157.
355. MOSHER D.F., DOYLE M.J., JAFFE E.A. Synthesis and secretion of thrombospondin by cultured human endothelial cells. J Cell Biol. 93:1982;343-348.
356. LEUNG L.L.K., NACHMAN R.L. Complex formation of platelet thrombospondin with fibrinogen. J Clin Invest. 70:1982;542-549.
357. TUSZYNSKI G.P., SRIVASTAVA S., SWITALSKA H.I., HOLT J.C., CIERNIEWSKI S.C., NIEWIAROWSKI S. The interaction of human platelet thrombospondin with fibrinogen. J Biol Chem. 260:1985;12240-12245.
358. BACON-BAGULEY T., KUDRYK B.J., WALZ D.A. Thrombospondin interaction with fibrinogen. Evidence for binding to the A alpha- and B beta-chains of fibrinogen. J Biol Chem. 262:1987;1927-1930.
359. AGAM G., GARTNER T.K., LEVIN A. Inhibition of platelet aggregation and lectin activity by oligamines. Thromb Res. 33:1984;245-257.
360. SATOH S., TAKAHASHI K., SAKURAGAWA N. Thrombospondin is an agglutinin of platelets. Thromb Res. 72:1993;509-517.
361. BLOMBÄCK B. Alfred L. Copley - The scientist and his contributions to our understanding of haemostasis, thrombosis and atherogenesis. Thromb Res. 66:1992;3-10.
362. ALVING B.M., CHUNG S.I., MURANO G., TANG D.B., FINLAYSON J.S. Rabbit fibrinogen: time course of constituent chain production in vivo. Arch Biochim Biophys. 217:1982;1-9.
363. VAN DE STOLPE A., JACOBS N., HAGE W.J., TERTOOLEN L., VAN KOOYK Y., NOVÁKOVÁ I.R.O., de WITTE T. Fibrinogen binding to ICAM-1 on EA. hy926 endothelial cells is dependent on an intact cytoskeleton. Thromb Haemost. 75:1996;182-189.
364. DEJANA E., ZANETTI A., CONTORTI G. Biochemical and functional characteristics of fibrinogen interaction with endothelial cells. Haemostasis. 18:1988;262-270.
365. ALTIERI D.C., BADER R., MANNUCCI P.M., EDGINGTON T.S. Oligospecificity of the cellular adhesion receptor MAC-1 encompasses an inducible recognition specificity for fibrinogen. J Cell Biol. 107:1988;1893-1900.
366. LANGUINO L.R., DUPERRAY A., JOGANIC K.J., FORNARO M., THORNTORN G.B., ALTIERI D.C. Regulation of leucocyte-endothelium interaction and leukocyte transendothelial migration by intercellular adhesion molecule 1-fibrinogen recognition. Proc Natl Acad Sci USA. 92:1995;1505-1509.
367. LEVEN R.M., SCHICK P.K., BUDZYNSKI A.Z. Fibrinogen biosynthesis in isolated guinea pig megakaryocytes. Blood. 65:1985;501-504.
368. ODDOUX C., GRIENINGER G. Fibrinogen assembly: insights from chicken hepatocytes. Hepatology. 19:1994;688-693.
369. UZAN G., COURTOIS G., STANKOVIC Z., CRABTREE G.R., MARGURIE G. Expression of the fibrinogen genes in rat megakaryocytes. Biochem Biophys Res Commun. 140:1986;543-549.
370. SHIMIZU A., SAITO Y., INADA Y. Distinctive role of histidine-16 of the Bβ chain of fibrinogen in the end-to-end association of fibrin. Proc Natl Acad Sci USA. 83:1986;591-593.
371. DOOLITTLE R.F., TAKAGI T., COTTRELL B.A. Platelet and plasma fibrinogens are identical gene products. Science. 185:1974;368-370.
372. GALANAKIS D.K., LANE B.P., SIMON S.R. Albumin modulates lateral assembly of fibrin polymers: Evidence of enhanced fine fibril formation and of unique synergism with fibrinogen. Biochemistry. 26:1987;2389-2400.
373. MOSESSON M.W., DiORIO J.P., SIEBENLIST K.R., WALL J.S., HAINFELD J.F. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood. 82:1993;1517-1521.
374. BUNCE L.A., SPORN L.A., FRANCIS C.W. Endothelial cell spreading on fibrin requires fibrinopeptide B cleavage and amino acid residues 15-42 of the β chain. J Clin Invest. 89:1992;842-850.
375. ERBAN J.K., WAGNER D.D. A 130-kDa protein on endothelial cells binds to amino acids 15-42 of the Bβ chain of fibrinogen. J Biol Chem. 267:1992;2451-2458.
376. CHUNG, D.W., HARRIS, J.E. and DAVIE, E.W. Nucleotide sequences of the three genes coding for human fibrinogen. In: Fibrinogen, Thrombosis, Coagulation and Fibrinolysis. Advances in Experimental Medicine and Biology, vol. 281. C.Y. Liu and S. Chien (eds.), pp. 39-48, Plenum Press, New York 1990.
377. BLOMBÄCK B., PROCYK R., ADAMSON L., HESSEL B. Factor XIII induced gelation of human fibrinogen - An alternative thiol enhanced, thrombin independent pathway. Thromb Res. 37:1985;613-628.
378. BLOMBÄCK, B., BANERJEE, D., CARLSSON, K., HAMSTEN, A., HESSEL, B., PROCYK, R., SILVEIRA, A. and ZACHARSKI, L. Native fibrin gel networks and factors influencing their formation in health and disease. In: Fibrinogen, Thrombosis, Coagulation and Fibrinolysis. C.Y. Liu and S. Chien (eds.), pp. 1-23, Plenum Press, New York 1990.
379. OLAISEN B., TEISBERG P., GEDDE-DAHL T. JR. Fibrinogen γ chain locus is on chromosome 4 in man. Hum Genet. 61:1982;24-26.
380. KANT J.A., FORNACE A.J. JR., SAXE D., SIMON M.I., McBRIDE O.W., CRABTREE G.R. Evolution and organization of the fibrinogen locus on chromosome 4: Gene duplication accompanied by transposition and inversion. Proc Natl Acad Sci USA. 82:1985;2344-2348.
381. PROCYK R., ADAMSON L., BLOCK M., BLOMBÄCK B. Factor XIII catalyzed formation of fibrinogen-fibronectin oligomers - a thiol enhanced process. Thromb Res. 40:1985;833-852.
382. PROCYK R., BLOMBÄCK B. Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin. Biochim Biophys Acta. 967:1988;304-313.
383. CRABTREE G.R., COMEAU C.M., FOWLKES D.M., FORNACE A.J. JR., MALLEY J.D., KANT J.A. Evolution and structure of the fibrinogen genes. Random insertion of introns or selective loss? J Mol Biol. 185:1985;1-19.
384. HENRY I., UZAN G., WEIL D., NICOLAS H., KAPLAN J.C., MARGUERIE C., KAHN A., JUNIEN C. The genes coding for Aα, Bβ, and γ-chains of fibrinogen Map to 4q2. Am J Hum Genet. 36:1984;760-768.
385. NICKERSON J.M., FULLER G.M. In vitro synthesis of rat fibrinogen: Identification of preAα, preBβ, and preγ polypeptides. Proc Natl Acad Sci USA. 78:1981;300-307.
386. YU S., SHER B., KUDRYK B., REDMAN C.M. Intracellular assembly of human fibrinogen. J Biol Chem. 258:1983;13407-13410.
387. YU S., SHER B., KUDRYK B., REDMAN C.M. Fibrinogen procursors. Order of assembly of fibrinogen chains. J Biol Chem. 259:1984;10574-10581.
388. YU, S., KUDRYK, B. and REDMAN, C. A scheme for the intracellular assembly of human fibrinogen. In: Fibrinogen-Fibrin Formation and Fibrinolysis. vol. 4. D.A. Lane, A. Henschen and M.K. Jasani (eds.), pp. 3-13, Walter de Gruyter Co., Berlin, New York 1986.
389. GRIENINGER G., HERZBERG K.M., PINDYCK J. Fibrinogen synthesis in serum-free hepatocyte cultures: Stimulation by glucocorticoids. Proc Natl Acad Sci USA. 75:1978;5506-5510.
390. CRABTREE G.R., KANT J.A. Coordinate accumulation of the mRNAs for the α, β, and γ chains of rat fibrinogen following defibrination. J Biol Chem. 257:1982;7277-7279.
391. NESBITT J.E., FULLER G.M. Transcription and translation are required for fibrinogen mRNA degradation in hepatocytes. Biochim Biophys Acta. 1089:1991;88-94.
392. OTTO J.M., GRENETT H.E., FULLER G.M. The coordinated regulation of fibrinogen gene transcription by hepatocyte-stimulating factor and dexamethasone. J Cell Biol. 105:1987;1067-1072.
393. PLANT P.W., GRIENINGER G. Noncoordinate synthesis of the fibrinogen subunits in hepatocytes cultured under hormone-deficient conditions. J Biol Chem. 261:1986;2331-2336.
394. KUDRYK B., OKADA M., REDMAN C.M., BLOMBÄCK B. Biosynthesis of dog fibrinogen: Characterization of nascent fibrinogen in the rough endoplasmic reticulum. Eur J Biochem. 125:1982;673-682.
395. HIROSE S., ODA K., IKEHARA Y. Tyrosine O-sulfation of the fibrinogen γB chain in primary cultures of rat hepatocytes. J Biol Chem. 263:1988;7426-7430.
396. YU S., KONG V., KUDRYK B., REDMAN C.M. Endogenous forms of fibrinogen in Hep G2 cells. Thromb Res. 46:1987;281-293.
397. ROY S., MUKHOPADHYAY G., REDMAN C.M. Regulation of fibrinogen assembly. Transfection of Hep G2 cells with Bβ cDNA specifically enhances synthesis of the three component chains of fibrinogen. J Biol Chem. 265:1990;6389-6393.
398. ROY S., YU S., BANERJEE D., OVERTON O., MUKHOPADHYAY G., ODDOUX C., GRIENINGER G., REDMAN C.M. Assembly and secretion of fibrinogen. Degradation of individual chains. J Biol Chem. 267:1992;23151-23158.
399. ROY S., OVERTON O., REDMAN C. Overexpression of any fibrinogen chain by Hep G2 cells specifically elevates the expression of the other two chains. J Biol Chem. 269:1994;691-695.
400. ROY S., PROCYK R., KUDRYK B.J., REDMAN C.M. Assembly and secretion of recombinant human fibrinogen. J Biol Chem. 266:1991;4758-4763.
401. HARTWIG R., DANISHEFSKY K.J. Studies on the assembly and secretion of fibrinogen. J Biol Chem. 266:1991;6578-6585.
402. BINNIE C.G., HETTASCH J.M., STRICKLAND E., LORD S.T. Characterization of purified recombinant fibrinogen: Partial phosphorylation of fibrinopeptide A. Biochemistry. 32:1993;107-113.
403. ROY S., KUDRYK B., REDMAN C.M. Secretion of biologically active recombinant fibrinogen by yeast. J Biol Chem. 270:1995;23761-23767.
404. NEEDHAM, A.E. Haemostatic mechanisms in invertebrata. In: The Haemostatic Mechanism in Man and Other Animals. Symposia of the Zoological Society of London, No. 27. R.G. MacFarlane (ed.), pp. 19-44, Academic Press, New York 1970.
405. IWANAGA S., MIATA T., TOKUNAGA F., MUTA T. Molecular mechanism of hemolymph clotting system in Limulus. Thromb Res. 68:1992;1-32.
406. FULLER G.M., DOOLITTLE R.F. Studies of invertebrate fibrinogen. II. Transformation of lobster fibrinogen into fibrin Biochemistry. 10:1971;1311-1315.
407. DOOLITTLE R.F., FULLER G.M. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies on lobster fibrinogen and fibrin. Biochim Biophys Acta. 263:1972;805-809.
408. DOOLITTLE R.F., RILEY M. The amino-terminal sequence of lobster fibrinogen reveals common ancestry with vitellogenins. Biochem Biophys Res Commun. 167:1990;16-19.
409. XU X., DOOLITTLE R.F. Presence of a vertebrate fibrinogen-like sequence in an echinoderm. Proc Natl Acad Sci USA. 87:1990;2097-2101.
410. WEISSBACH L., GRIENINGER G. Bipartite mRNA for chicken α-fibrinogen potentially encodes an amino acid sequence homologous to β- and γ-fibrinogens. Proc Natl Acad Sci USA. 87:1990;5198-5202.
411. PAN Y., DOOLITTLE R.F. cDNA sequence of a second fibrinogen α chain in lamprey: An archetypal version alignable with full-length β and γ chains. Proc Natl Acad Sci USA. 89:1992;2066-2070.
412. DOOLITTLE R.F., BLOMBÄCK B. Amino-acid sequence investigations of fibrinopeptides from various mammals: Evolutionary implications. Nature. 202:1964;147-152.
413. TEGER-NILSSON A.-C., BLOMBÄCK B. Rate of thrombin-fibrinogen reaction in some mammalian species. Thromb Res. 5:1974;223-233.
414. DOOLITTLE R.F., FENG D.-F., TSANG S., CHO G., LITTLE E. Determining divergence times of the major Kingdoms of living organisms with a protein clock. Science. 271:1996;470-477.
415. AL-MONDHIRY H., EHMANN C.W. Congenital afibrinogenemia. Am J Hematol. 46:1994;343-347.
416. UZAN G., COURTOIS G., BESMOND C., FRAIN M., SALA-TREPAT J., KAHN A., MARGUERIE G. Analysis of fibrinogen genes in patients with congenital afibrinogenemia. Biochem Biophys Res Commun. 120:1984;376-383.
417. ZHENG ZHI, ASHTON R.W., NI F., SCHERAGA H.A. Thrombin hydrolysis of an N-terminal peptide from fibrinogen Lille: Kinetic and NMR studies. Biochemistry. 31:1992;4226-4231.
418. HIGGINS D.L., SHAFER J.A. Fibrinogen Petoskey, a dysfibrinogenemia characterized by replacement of Arg-Aα16 by a histidyl residue. J Biol Chem. 256:1981;12013-12017.
419. SORIA, J., SORIA, C., SAMAMA, M., HENSCHEN, A. and SOUTHAN, C. Detection of fibrinogen abnormality in dysfibrinogenemia. Special report on fibrinogen Metz characterized by an amino acid substitution located at the peptide bond cleaved by thrombin. In: Fibrinogen - Recent Biochemical and Medical Aspects. vol. 1. A. Henschen et al. (eds.), pp. 129-143. Walter de Gruyter & Co., Berlin, New York 1981.
420. KOOPMAN J., HAVERKATE F., GRIMBERGEN J., ENGESSER L., NOVÁKOVÁ I., KERST A.F.J.A., LORD S.T. Abnormal fibrinogens IJmuiden (Bβ Arg 14→Cys) and Nijmegen (Bβ Arg 44→Cys) form disulfide-linked fibrinogen-albumin complexes. Proc Natl Acad Sci USA. 89:1992;3478-3482.
421. LIU C.Y., KOEHN J.A., MORGAN F.J. Characterization of fibrinogen New York I. A dysfunctional fibrinogen with a deletion of Bβ(9-72) corresponding exactly to exon 2 of the gene. J Biol Chem. 260:1985;4390-4396.
422. LIU, C.Y., WALLÉN, P. and HANDLEY, D.A. Fibrinogen New York I. The structural, functional, and genetic defects and an hypothesis of the role of fibrin in the regulation of coagulation and fibrinolysis. In: Fibrinogen, Fibrin Formation and Fibrinolysis. vol. 4, pp. 79-90. D.A. Lane, A. Henschen and M.K. Jasam (eds.), Walter de Gruyter, Berlin 1986.
423. KAUDEWITZ, H., HENSCHEN, A., SORIA, C. and SORIA, J., BERTRAND, O. and HEATON, D. The molecular defect of the genetically abnormal fibrinogen Christchurch II. In: Fibrinogen and Its Derivatives. G. Müller-Berghaus, U. Scheefers-Borchel, E. Selmayr and A. Henschen (eds.), pp. 31-36, Elsevier Science Publ. BV., Amsterdam, New York-Oxford 1986.
424. SOBEL J.H., TRAKHT I., WU H.Q., RUDCHENKO S., EGBRING R. α-chain cross-linking in fibrin(ogen) Marburg. Blood. 86:1995;989-1000.
425. COLLET J.-P., SORIA J., MIRSHAHI M., HIRSCH M., DAGONNET F.B., CAEN J., SORIA C. Dusart Syndrome: A new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood. 82:1993;2462-2469.
426. WADA Y., LORD S.T. A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα 554 Arg-→Cys) in two unrelated kindred, Dusart and Chapel Hill III. Blood. 84:1994;3709-3714.
427. CARR M.E. JR., BLATT P.M., ROBERTS H.R., BROOKER J.Z., HERMANS J. Detection of an abnormal plasma clot structure by a simple rigidity assay. Thromb Haemost. 42:1979;965-971.
428. HAVERKATE F., SAMAMA M. Familial dysfibrinogenemia and thrombophilia. Thromb Haemost. 73:1995;151-161.
429. MÉNACHÉ D. Constitutional and familial abnormal fibrinogen. Thromb Diath Haemorrh. 13(Suppl.):1964;173-185.
430. HESSEL B., SILVEIRA A.M.V., CARLSSON K., OKSA H., RASI V., VAHTERA E., PROCYK R., BLOMBÄCK B. Fibrinogenemia Tampere - A dysfibrinogenemia with defective gelation and thromboembolic disease. Thromb Res. 78:1995;323-339.
431. DAHL O.E., PEDERSEN T., KIERULF P., WESTVIK Å.-B., LUND P., ARNESEN H., SELJEFLOT I., ABDELNOOR M., LYBERG T. Sequential intrapulmonary and systemic activation of coagulation and fibrinolysis during and after total hip replacement surgery. Thromb Res. 70:1993;451-458.
432. ERNST E. Plasma fibrinogen-an independent cardiovascular risk factor. J Intern Med. 227:1990;365-372.
433. FATAH K., HAMSTEN A., BLOMBÄCK B., BLOMBÄCK M. Fibrin gel network characteristics and coronary heart disease: relations to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary atherosclerosis. Thromb Haemost. 68:1992;130-135.
434. McDONAGH J. Suppression of plasminogen binding to fibrin by high fibrinogen: A mechanism for how high fibrinogen enhances the risk of thrombosis. CML - Thrombosis. 3:1993;II-XIX.
435. WILLIAMS S., FATAH K., IVERT T., BLOMBÄCK M. The effect of acetylsalicylic acid on fibrin gel lysis by tissue plasminogen activator. Blood Coag Fibrinol. 6:1995;718-725.
436. BJORNSSON T.D., SCHNEIDER D.E., BERGER H. JR. Aspirin acetylates fibrinogen and enhances fibrinolysis. Fibrinolytic effect is independent of changes in plasminogen activator levels. J Pharmacol Exp Ther. 250:1989;154-161.
437. REININGER A.J., HEINZMANN U., REININGER C.G., FRIEDRICH P., WURZINGER L.J. Flow mediated fibrin thrombus formation in an endothelium-lined model of arterial branching. Thromb Res. 74:1994;629-641.
438. TIPPE A., MÜLLER-MONHSSEN H. Shear dependence of the fibrin coagulation kinetics in vitro. Thromb Res. 72:1993;379-388.
439. DAVIES M.J. The contribution of thrombosis to the clinical expression of coronary atherosclerosis. Thromb Res. 82:1996;1-32.
440. FU Y., CAO Y., HERTZBERG K.M., GRIENINGER G. Fibrinogen α genes: Conservation of bipartite transcripts and carboxy-terminal-extended α subunits in vertebrates. Genomic. 30:1995;71-76.
441. MEH D.A., SIEBENLIST K.R., GALANAKIS D.K., BERGTROM G., MOSESSON M.W. The dimeric Aα chain composition of dysfibrinogenemic molecules with mutations at Aα 16. Thromb Res. 78:1995;531-539.
442. KOOPMAN J., HAVERKATE F., LORD S.T., GRIMBERGEN J., MANNUCCI P.M. Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of Bβ68Ala→Thr. J Clin Invest. 90:1992;238-244.
443. KOOPMAN J., HAVERKATE F., GRIMBERGEN J., EGBRING R., LORD S.T. Fibrinogen Marburg: A homozygous case of dysfibrinogenemia, lacking amino acids Aα 461-610 (Lys 461 AAA→STOP TAA). Blood. 80:1992;1972-1979.